This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The Group VIA phospholipase A(2) (iPLA(2)[unreadable]) hydrolyzes glycerophospholipids at the sn-2-position to yield a free fatty acid and a 2-lysophospholipid, and iPLA(2)[unreadable] has been reported to participate in apoptosis, phospholipid remodeling, insulin secretion, transcriptional regulation, and other processes. Induction of endoplasmic reticulum (ER) stress in [unreadable]-cells and vascular myocytes with SERCA inhibitors activates iPLA(2)[unreadable], resulting in hydrolysis of arachidonic acid from membrane phospholipids, by a mechanism that is not well understood.